Abstract:
:In order to clarify the impact of Ca-binding sites (Ca1 and 2) on the conformational stability of neutral proteases (NPs), we have analyzed the thermal, pH and organic solvent stability of a NP variant, V189P/A195E/G203D/A268E (Q-mutant), from Salinovibrio proteolyticus. This mutant has shown to bind calcium more tightly than the wild-type (WT) at Ca1 and to possess Ca2. Q-mutant was resisted against autolysis, thermoinactivation and pH denaturation in a Ca-dependent manner and exhibited better activity in organic solvents compared to the WT enzyme. These results imply that Ca1 and Ca2 are important for the conformational stability of NPs.
journal_name
BMB Repjournal_title
BMB reportsauthors
Asghari SM,Khajeh K,Dalfard AB,Pazhang M,Karbalaei-Heidari HRdoi
10.5483/BMBRep.2011.44.10.665subject
Has Abstractpub_date
2011-10-01 00:00:00pages
665-8issue
10eissn
1976-6696issn
1976-670Xjournal_volume
44pub_type
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